Chemical Exchange at the Trinuclear Copper Center of Small Laccase from Streptomyces coelicolor
Autor: | Rubin Dasgupta, Karthick Babu Sai Sankar Gupta, Marcellus Ubbink, Huub J. M. de Groot, Edgar J. J. Groenen, Gerard W. Canters, Faezeh Nami |
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Jazyk: | angličtina |
Rok vydání: | 2020 |
Předmět: |
Magnetic Resonance Spectroscopy
Biophysics chemistry.chemical_element Streptomyces coelicolor Crystal structure Overpotential law.invention 03 medical and health sciences chemistry.chemical_compound Paramagnetism 0302 clinical medicine law Imidazole Electron paramagnetic resonance Histidine 030304 developmental biology 0303 health sciences biology Chemistry Biophysical Letter Laccase Electron Spin Resonance Spectroscopy biology.organism_classification Copper Crystallography 030217 neurology & neurosurgery |
Zdroj: | Biophysical Journal Biophysical Journal, 119(1), 9-14 |
ISSN: | 1542-0086 0006-3495 |
Popis: | The trinuclear copper center (TNC) of laccase reduces oxygen to water with very little overpotential. The arrangement of the coppers and ligands in the TNC is known to be from many crystal structures, yet information about possible dynamics of the ligands is absent. Here, we report dynamics at the TNC of small laccase from Streptomyces coelicolor using paramagnetic NMR and electron paramagnetic resonance spectroscopy. Fermi contact-shifted resonances tentatively assigned to histidine Hδ1 display a two-state chemical exchange with exchange rates in the order of 100 s−1. In the electron paramagnetic resonance spectra, at least two forms are observed with different gz-values. It is proposed that the exchange processes reflect the rotational motion of histidine imidazole rings that coordinate the coppers in the TNC. Graphical Abstract |
Databáze: | OpenAIRE |
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